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4a subunit
1 Department of Biomedical Sciences, College of Veterinary Medicine and Biomedical Sciences, and 2 Department of Chemistry, College of Natural Sciences, Colorado State University, Fort Collins, Colorado 80526, USA
3 Department of Chemistry and Biochemistry, College of Arts and Sciences, New Mexico State University, Las Cruces, New Mexico 88003, USA
(RECEIVED October 7, 2005; FINAL REVISION November 4, 2005; ACCEPTED November 8, 2005)
Ca2+ channel 
subunits regulate trafficking and gating (opening and closing) of voltage-dependent Ca2+ channel 
1 subunits. Based on primary sequence comparisons, they are thought to be modular structures composed of five domains (A–E) that are related to the large family of membrane associated guanylate-kinase (MAGUK) proteins. The crystal structures of the subunit core, B–D, domains have recently been reported; however, very little is known about the structures of the A and E domains. The N-terminal A domain is a hypervariable region that differs among the four subtypes of Ca2+ channel subunits (1–4). Furthermore, this domain undergoes alternative splicing to create multiple N-terminal structures within a given gene class that have distinct effects on gating. We have solved the solution structure of the A domain of the human 4a subunit, a splice variant that we have shown previously to have 1 subunit subtype-specific effects on Ca2+ channel trafficking and gating.
Keywords: Ca2+ channel; 4a subunit; nuclear magnetic resonance; alternative splicing; membrane-associated guanylate-kinase protein; protein structure; domains and motifs; exon/intron relationship; ion channel
Abbreviations: AID, 1 subunit interaction domain • DSS, 2-2-Di-methyl-2-silapentane-5-sulfonic acid • GK, guanylate-kinase • HSQC, heteronuclear single quantum coherence • MAGUK, membrane associated guanylate-kinase • NMR, nuclear magnetic resonance • NOE, nuclear Overhauser effect • NOESY, NOE spectroscopy • PCR, polymerase chain reaction • RMSD, root-mean-square deviation • SH3, src homology 3 • TOCSY, total correlation spectroscopy
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051894506.
Reprint requests to: William A. Horne, Department of Biomedical Sciences, 1617 Campus Delivery, Colorado State University, Fort Collins, CO 80523, USA; e-mail: bill.horne{at}colostate.edu; fax: (970) 491-7907.
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